chymotrypsin

Chymotrypsin (Chymotrypsin A) is a serine protease synthesized by the pancreas, which cleaves protein chains on the carboxyl side of aromatic amino acids.

Chymotrypsinogen is an inactive precursor of Chymotrypsin . Chymotrypsin is a serine protease produced by the pancreas [1] [2] .

Alpha 1 Antichymotrypsin, Human Plasma is an inhibitor of serine proteases. This compound is present in amyloid lesions associated with Alzheimer's disease and can be utilized in Alzheimer's research.

Aprotinin (Traskolan) is a broad-spectrum serine protease (BPTI) inhibitor that inhibits the activity of a number of different esterases and proteases. Aprotinin is an antifibrinolytic agent used to minimize hemorrhage during complex surgical procedures.

Leupeptin is a competitive protease inhibitor produced by actinomycetes. Leupeptin can inhibit cysteine, serine and threonine peptidases. Leupeptin inhibits serine proteinases (trypsin (Ki=3.5 nM), plasmin (Ki= 3.4 nM), porcine kallikrein), and cysteine p

RETF-4NA acetate is a sensitive, specific substrate for chymotrypsin.

The bentiromide test is an excellent means of confirming the diagnosis of pancreatic exocrine insufficiency by outpatient test of chymotrypsin function[1]. Bentiromide is a peptide which is broken down in the pancreas by chymotrypsin.

Z-LLL-AMC is a fluorogenic substrate for the chymotrypsin-like activity of the 26S proteasome or 20S proteolytic core. Chymotrypsin-like activity can be quantified by fluorescent detection of free AMC (also known as 7-amino-4-methylcoumarin), which is excited at 340-360 nm and emits at 440-460 nm. Z-LLL-AMC is typically used in cell lysates after experimental treatment.

Proteasome-activating peptide 1 TFA is a potent activator of the proteasome, enhancing chymotrypsin-like proteasomal catalytic activity and increasing proteolytic rates both in vitro and in culture. It also inhibits protein aggregation in cellular models of amyotrophic lateral sclerosis (ALS) [1].

Suc-Ala-Ala-Pro-Phe-SBzl serves as a substrate for rat intestinal mast cell protease (RMCP I), rat skeletal muscle mast cell protease (RMCP II), and Chymotrypsin, and undergoes hydrolysis by glycine (R208G) [1] [2].

Z-Leu-Leu-Tyr-COCHO is a potent inhibitor of chymotrypsin-like activity, with a Ki value of 3.0 nM [1].

Z-Gly-Pro-Phe-Leu-CHO (Z-GPFL-CHO) is a tetrapeptide aldehyde that acts as a selective and potent proteasome inhibitor, with inhibition constants (Ki) of 1.5 µM for branched-chain amino acid-preferred, 2.3 µM for small neutral amino acid-preferred, and 40.5 µM for chymotrypsin-like activities, and an inhibitory concentration (IC50) of 3.1 µM for peptidyl-glutamyl peptide hydrolyzing activity [1].

Proteasome-activating peptide 1 enhances chymotrypsin-like proteasomal catalytic activity, boosting proteolytic rates both in vitro and within cultured cells. Additionally, it inhibits protein aggregation in a cellular model of amyotrophic lateral sclerosis [1].

Suc-Leu-Leu-Val-Tyr-AMC is a fluorescent substrate for the 20S proteasome, as well as other chymotrypsin-like proteases (20S-proteasome chymotrypsin).

Gluten exorphin C is an opioid peptide derived from wheat gluten, with IC50 values of 40 μM for μ opioid and 13.5 μM for δ opioid activities in the GPI and MVD assays, respectively. Isolated from the pepsin-trypsin-chymotrypsin digest of wheat gluten, it is considered a δ-opioid receptor-selective ligand.